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Information on EC 2.7.1.185 - mevalonate 3-kinase
for references in articles please use BRENDA:EC2.7.1.185
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.1 Phosphotransferases with an alcohol group as acceptor
2.7.1.185 mevalonate 3-kinase
IUBMB Comments
Mevalonate 3-kinase and mevalonate-3-phosphate-5-kinase (EC 2.7.1.186) act sequentially in an alternate mevalonate pathway in the archaeon Thermoplasma acidophilum. Mevalonate 3-kinase is different from mevalonate kinase, EC 2.7.1.36, which transfers phosphate to position 5 of (R)-mevalonate and is part of the classical mevalonate pathway in eukaryotes and archaea.
The expected taxonomic range for this enzyme is: Archaea, Bacteria
- 2.7.1.185
- acidophilum
-
thermoplasma
-
isopentenyl
-
isoprenoids
- pyrophosphate
- decarboxylases
-
picrophilus
- archaea
- torridus
- cholesterol
- synthesis
showSynonyms
mevalonate 3-kinase, mevalonate-3-kinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
M3K
mevalonate 3-kinase
mevalonate-3-kinase
PtM3K
PTO1356
Ta1305
TacM3K
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
-
-
-
-
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
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ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
-
-
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
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-
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
-
-
ATP + (R)-mevalonate = ADP + (R)-3-phosphomevalonate
catalytic mechanism of this rare type of decarboxylase, the enzyme is bifunctional showing the reactions of diphosphomevalonate decarboxylase (EC 4.1.1.33) and mevalonate 3-kinase (EC 2.7.1.185), overview
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
mevalonate pathway III (Thermoplasma)
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SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-mevalonate 3-phosphotransferase
Mevalonate 3-kinase and mevalonate-3-phosphate-5-kinase (EC 2.7.1.186) act sequentially in an alternate mevalonate pathway in the archaeon Thermoplasma acidophilum. Mevalonate 3-kinase is different from mevalonate kinase, EC 2.7.1.36, which transfers phosphate to position 5 of (R)-mevalonate and is part of the classical mevalonate pathway in eukaryotes and archaea.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
Substrates: the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
Products: -
Products: -
?
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
Picrophilus oshimae ATCC 700027
Substrates: the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
Products: -
Products: -
?
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
Picrophilus oshimae DSM 9790
Substrates: the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
Products: -
Products: -
?
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
Picrophilus oshimae JCM 10055
Substrates: the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
Products: -
Products: -
?
ATP + (R)-2,3-dihydroxyisovalerate
ADP + (R)-2-hydroxy-3-phosphoisovalerate
Picrophilus oshimae NBRC 100828
Substrates: the Picrophilus torridus mevalonate-3-kinase (M3K) exhibits adenosine triphosphate (ATP) hydrolysis activity when mixed with (R)-2,3-dihydroxyisovalerate (DHIV), indicating phosphorylation activity towards DHIV
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae ATCC 700027
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae DSM 9790
Substrates: key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae DSM 9790
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae JCM 10055
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae NBRC 100828
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: mevalonate-3-kinase and mevalonate-3-phosphate-5-kinase act sequentially in a putative alternate mevalonate pathway in Thermoplasma acidophilum
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: the enzyme is part of a putative alternate mevalonate pathway in Thermoplasma acidophilum
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
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ATP + 3-hydroxyisovalerate
ADP + phosphate + isobutene + CO2
Substrates: the potential of the enzyme in isobutene formation is due to the conversion of 3-hydroxyisovalerate to an unstable 3-phosphate intermediate that undergoes consequent spontaneous decarboxylation to form isobutene
Products: -
Products: -
?
ATP + 3-hydroxyisovalerate
ADP + phosphate + isobutene + CO2
Picrophilus oshimae DSM 9790
Substrates: the potential of the enzyme in isobutene formation is due to the conversion of 3-hydroxyisovalerate to an unstable 3-phosphate intermediate that undergoes consequent spontaneous decarboxylation to form isobutene
Products: -
Products: -
?
additional information
?
-
Substrates: a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
Products: -
Products: -
?
additional information
?
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Picrophilus oshimae ATCC 700027
Substrates: a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
Products: -
Products: -
?
additional information
?
-
Picrophilus oshimae DSM 9790
Substrates: a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
Products: -
Products: -
?
additional information
?
-
Picrophilus oshimae JCM 10055
Substrates: a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
Products: -
Products: -
?
additional information
?
-
Picrophilus oshimae NBRC 100828
Substrates: a first reaction strategy is the activaion of (R)-2,3-dihydroxyisovalerate (DHIV) to 3-phospho-DHIV using M3K followed by dehydration by PpManR, StPutD or other sugar acid dehydratases. A second strategy is to use M3K and/or mevalonate decarboxylase (MVD) to convert DHIV to isobutyraldehyde, which can be an alternative pathway for isobutanol biosynthesis
Products: -
Products: -
?
additional information
?
-
-
Substrates: NMR analysis of the product
Products: -
Products: -
?
additional information
?
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Substrates: NMR analysis of the product
Products: -
Products: -
?
additional information
?
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Substrates: NMR analysis of the product
Products: -
Products: -
?
additional information
?
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Substrates: NMR analysis of the product
Products: -
Products: -
?
additional information
?
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Substrates: NMR analysis of the product
Products: -
Products: -
?
additional information
?
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
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Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
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Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
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Substrates: substrate specificity, overview
Products: -
Products: -
?
additional information
?
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Substrates: substrate specificity, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae ATCC 700027
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae DSM 9790
Substrates: key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae DSM 9790
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae JCM 10055
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Picrophilus oshimae NBRC 100828
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: mevalonate-3-kinase and mevalonate-3-phosphate-5-kinase act sequentially in a putative alternate mevalonate pathway in Thermoplasma acidophilum
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: the enzyme is part of a putative alternate mevalonate pathway in Thermoplasma acidophilum
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
ATP + (R)-mevalonate
ADP + (R)-3-phosphomevalonate
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
8.5
the monomeric and dimeric forms have equal activity under optimal conditions
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
pH 7.0: about 75% of maximal activity, pH 9.5: about 85% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
55
the monomeric and dimeric forms have equal activity under optimal conditions
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
40°C: about 55% of maximal activity, 60°C: about 95% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
evolution
-
mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
-
evolution
-
mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
-
evolution
-
mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
-
evolution
-
mevalonate 3-kinase is an enzyme involved in the modified mevalonate pathway specific to limited species of thermophilic archaea
-
malfunction
-
site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
malfunction
-
site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
-
malfunction
-
site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
-
malfunction
-
site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
-
malfunction
-
site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step
-
metabolism
key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
metabolism
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
metabolism
Picrophilus oshimae DSM 9790
-
key enzyme of the Thermoplasma acidophilum-type mevalonate pathway
-
metabolism
-
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
-
metabolism
-
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
-
metabolism
-
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
-
metabolism
-
mevalonate 3-kinase plays a key role in a recently discovered modified mevalonate pathway specific to thermophilic archaea of the order Thermoplasmatales, pathway overview. In the pathway called modified MVA pathway II, mevalonate (MVA) is phosphorylated at the 3-hydroxyl group to yield 3-phosphomevalonate (MVA-3-P) by the action of mevalonate 3-kinase (M3K) rather than at the 5-hydroxyl group as in the reaction of MVK (EC 2.7.4.2). M3K is also homologous to diphosphomevalonate decarboxylase (DMD, EC 4.1.1.33). After the formation of MVA-3-P, another kinase, MVA-3-P 5-kinase (M3P5K), catalyzes its 5-phosphorylation, and a subsequent decarboxylation is catalyzed by another DMD homologue, 3,5-bisphosphomevalonate decarboxylase (BMD), to give isopentenyl phosphate (IP). IP is then phosphorylated by isopentenyl phosphate kinase (IPK) to yield isopentenyl diphosphate (IPP). The M3K enzyme is homologous to diphosphomevalonate decarboxylase, which is involved in the widely distributed classical mevalonate pathway, and to phosphomevalonate decarboxylase, which is possessed by halophilic archaea and some Chloroflexi bacteria. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate
-
physiological function
mevalonate-3-kinase and mevalonate-3-phosphate-5-kinase act sequentially in a putative alternate mevalonate pathway in Thermoplasma acidophilum
physiological function
the enzyme is part of a putative alternate mevalonate pathway in Thermoplasma acidophilum
physiological function
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
physiological function
-
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
physiological function
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
physiological function
-
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
-
physiological function
-
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
-
physiological function
Picrophilus oshimae DSM 9790
-
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
-
physiological function
-
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
-
physiological function
-
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
-
physiological function
-
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
-
physiological function
-
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme
-
physiological function
-
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
-
physiological function
-
mevalonate 3-kinase catalyzes the ATP-dependent 3-phosphorylation of mevalonate but does not catalyze the subsequent decarboxylation as related decarboxylases do
-
physiological function
Picrophilus oshimae ATCC 700027
-
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
-
physiological function
Picrophilus oshimae JCM 10055
-
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
-
physiological function
Picrophilus oshimae NBRC 100828
-
the enzyme is specialized as a mevalonate 3-kinase catalyzing the first step of the mevalonate decarboxylation (MVD) reaction
-
additional information
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
additional information
-
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
additional information
-
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
-
additional information
-
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
-
additional information
-
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
-
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
-
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
-
additional information
-
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD (EC 4.1.1.33) and M3K, overview
-
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
-
additional information
-
comparison between the substrate-complex crystal structure of TacM3K (PDB ID 4RKS) and that of Sulfolobus solfataricus DMD (SsoDMD, PDB ID 5GMD) revealing interesting differences in the structures of the active sites. The steric hindrance introduced by Glu140 seems responsible for excluding larger substrates, such as MVA 5-phosphate and MVA 5-diphosphate, from the active site of TacM3K
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MV3K_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)
324
0
36791
Swiss-Prot
-
MV3K_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
318
0
35201
Swiss-Prot
-
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
the monomeric and dimeric forms have equal activity under optimal conditions
monomer
the monomeric and dimeric forms have equal activity under optimal conditions
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with (R)-5-diphosphomevalonate and adenosine 5'-O-(3-thio)triphosphate or with (R)-5-diphosphomevalonate and ADP, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution
-
analysis of the substrate-complex crystal structure of TacM3K (PDB ID 4RKS)
hanging drop method, crystal structure of mevalonate-3-kinase in the apo form, and with bound substrates is determined and compared to mevalonate diphosphate decarboxylase structures. The crystal structure of mevalonate-3-kinase provides insight into the mechanism of mevalonate diphosphate decarboxylase. Despite sharing nearly identical overall folds, important active site differences are identified. Glu140 in the center of the mevalonate-3-kinase active site is responsible for binding mevalonate while excluding mevalonate 5-diphosphate, Arg185/Ser105 catalyze phosphate transfer, and an invariant Asp/Lys pair previously thought to be responsible for phosphorylation in mevalonate diphosphate decarboxylase, is missing in mevalonate-3-kinase and replaced by non-essential Thr275/Leu18. A model is proposed in which mevalonate-3-kinase and mevalonate diphosphate decarboxylase both phosphorylate by stabilizing a phosphotransfer transition state (mevalonate-3-kinase via Arg185/Ser105, mevalonate diphosphate decarboxylase via Lys188), suggesting the invariant Asp/Lys pair unique to mevalonate diphosphate decarboxylase may be critical for the decarboxylation step rather than phosphorylation
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D281A
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
D281N
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
D281T
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
D281V
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
D281A
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281N
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281T
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281V
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281A
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281N
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281T
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281V
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281A
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281N
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281T
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281V
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281A
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281N
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281T
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
D281V
-
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation
-
E140G
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
E140S
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
L18A
kcat/KM for (R)-mevalonate is 4.4% compared to the wild-type value
R185K
kcat/KM for (R)-mevalonate is 0.5% compared to the wild-type value
S105A
kcat/KM for (R)-mevalonate is 10.3% compared to the wild-type value
T275A
kcat/KM for (R)-mevalonate is 25.6% compared to the wild-type value
E140G
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140S
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140G
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140S
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140G
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140S
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140G
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
E140S
-
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate
-
additional information
additional information
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
-
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
-
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
-
additional information
-
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene Ta1305, the pBAD-TacM plasmid series contains the genes of M3K, M3P5K, BMD, and IPK for the expression of part of modified MVA pathway II. Although the M3K, M3P5K, and IPK genes are derived from Thermoplasma acidophilum, various BMD genes have been utilized for plasmid construction. Recombinant expression of His-tagged enzyme in Escherichia coli strain BL21
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
isobutene production rates are 507 pmol/min*g cells using Escherichia coli cells expressing the enzyme and 2880 pmol/min*mg protein with the purified histidine-tagged enzyme. Isobutene is a small, highly reactive molecule, used extensively as a platform chemical to manufacture a wide variety of products including fuel additives, rubbers, and speciality chemicals
synthesis
Picrophilus oshimae DSM 9790
-
isobutene production rates are 507 pmol/min*g cells using Escherichia coli cells expressing the enzyme and 2880 pmol/min*mg protein with the purified histidine-tagged enzyme. Isobutene is a small, highly reactive molecule, used extensively as a platform chemical to manufacture a wide variety of products including fuel additives, rubbers, and speciality chemicals
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vinokur, J.M.; Korman, T.P.; Cao, Z.; Bowie, J.U.
Evidence of a novel mevalonate pathway in archaea
Biochemistry
53
4161-4168
2014
Thermoplasma acidophilum (Q9HIN1), Thermoplasma acidophilum
brenda
Azami, Y.; Hattori, A.; Nishimura, H.; Kawaide, H.; Yoshimura, T.; Hemmi, H.
(R)-Mevalonate 3-phosphate is an intermediate of the mevalonate pathway in Thermoplasma acidophilum
J. Biol. Chem.
289
15957-15967
2014
Thermoplasma acidophilum (Q9HIN1)
brenda
Rossoni, L.; Hall, S.J.; Eastham, G.; Licence, P.; Stephens, G.
The putative mevalonate diphosphate decarboxylase from Picrophilus torridus is in reality a mevalonate-3-kinase with high potential for bioproduction of isobutene
Appl. Environ. Microbiol.
81
2625-2634
2015
Picrophilus oshimae (Q6KZB1), Picrophilus oshimae DSM 9790 (Q6KZB1)
brenda
Vinokur, J.M.; Korman, T.P.; Sawaya, M.R.; Collazo, M.; Cascio, D.; Bowie, J.U.
Structural analysis of mevalonate-3-kinase provides insight into the mechanisms of isoprenoid pathway decarboxylases
Protein Sci.
24
212-220
2015
Thermoplasma acidophilum (Q9HIN1), Thermoplasma acidophilum
brenda
Motoyama, K.; Sobue, F.; Kawaide, H.; Yoshimura, T.; Hemmi, H.
Conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase by single amino acid mutations
Appl. Environ. Microbiol.
85
e00256-19
2019
Thermoplasma acidophilum (Q9HIN1), Thermoplasma acidophilum, Thermoplasma acidophilum JCM 9062 (Q9HIN1), Thermoplasma acidophilum ATCC 25905 (Q9HIN1), Thermoplasma acidophilum NBRC 15155 (Q9HIN1), Thermoplasma acidophilum AMRC-C165 (Q9HIN1)
brenda
Motoyama, K.; Unno, H.; Hattori, A.; Takaoka, T.; Ishikita, H.; Kawaide, H.; Yoshimura, T.; Hemmi, H.
A single amino acid mutation converts (R)-5-diphosphomevalonate decarboxylase into a kinase
J. Biol. Chem.
292
2457-2469
2017
Saccharolobus solfataricus, Saccharolobus solfataricus P2, Saccharolobus solfataricus DSM 1617, Saccharolobus solfataricus ATCC 35092, Saccharolobus solfataricus JCM 11322
brenda
Oki, K.; Lee, F.S.; Mayo, S.L.
Attempts to develop an enzyme converting DHIV to KIV
Protein Eng. Des. Sel.
32
261-270
2019
Picrophilus oshimae (Q6KZB1), Picrophilus oshimae DSM 9790 (Q6KZB1), Picrophilus oshimae ATCC 700027 (Q6KZB1), Picrophilus oshimae JCM 10055 (Q6KZB1), Picrophilus oshimae NBRC 100828 (Q6KZB1)
brenda
EXTERNAL LINKS (specific for EC-Number 2.7.1.185)
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